1rgx

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Revision as of 23:28, 20 November 2007

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spinqualitylabelsall models 1rgx, resolution 1.787Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of resisitin

Overview

Resistin, founding member of the resistin-like molecule (RELM) hormone, family, is secreted selectively from adipocytes and induces liver-specific, antagonism of insulin action, thus providing a potential molecular link, between obesity and diabetes. Crystal structures of resistin and RELMbeta, reveal an unusual multimeric structure. Each protomer comprises a, carboxy-terminal disulfide-rich beta-sandwich "head" domain and an, amino-terminal alpha-helical "tail" segment. The alpha-helical segments, associate to form three-stranded coiled coils, and surface-exposed, interchain disulfide linkages mediate the formation of tail-to-tail, hexamers. Analysis of serum samples shows that resistin circulates in two, distinct assembly states, likely corresponding to hexamers and trimers., Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in, pancreatic-insulin clamp studies reveals substantially more potent effects, on hepatic insulin sensitivity than those observed with wild-type, resistin. This result suggests that processing of the intertrimer, disulfide bonds may reflect an obligatory step toward activation.

About this Structure

1RGX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Disulfide-dependent multimeric assembly of resistin family hormones., Patel SD, Rajala MW, Rossetti L, Scherer PE, Shapiro L, Science. 2004 May 21;304(5674):1154-8. PMID:15155948

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